PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation

ABSTRACT: Poly(ADP-ribose) polymerase 1 (PARP1) plays crucial roles in recruiting DNA repair proteins through its activity - poly(ADP-ribosyl)ation (PARylation). The enrichment of DNA repair proteins at sites of DNA damage has been described as the formation of a biomolecular condensate. However, it remains unclear how PARP1 and PARylation contribute to the formation and organization of DNA repair condensates. We find that PARP1 readily forms viscous condensates in vitro; this depends on DNA and PARP1 three zinc finger domains. PARylation enhances the formation and internal dynamics of PARP1 condensates. DNA and single-strand break repair proteins partition in these condensates in different patterns. FUS enrichment is enhanced upon PARylation whereas Polβ partitioning is not. XRCC1 and LigIII displa

SUBMITTER: Christopher Chin Sang 

PROVIDER: S-SCDT-10_1038-S44319-024-00285-5 | biostudies-other |

REPOSITORIES: biostudies-other